Laccase component of the Ceriporiopsis subvermispora lignin-degrading system

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Lignin-degrading peroxidases from the genome of the selective ligninolytic fungus Ceriporiopsis subvermispora*

Background: The first genome of a selective lignin-degrader is available. Results: Its screening shows 26 peroxidase genes, and five were heterologously expressed and catalytic properties investigated. Conclusion: Two new peroxidases oxidize simple and dimeric lignin models and efficiently depolymerize lignin. Significance: Although lignin peroxidase and versatile peroxidase had not been report...

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Properties of laccase isoenzymes produced by the basidiomycete Ceriporiopsis subvermispora.

Laccase is one of the ligninolytic enzymes found in liquid cultures of the fungus Ceriporiopsis subvermispora in defined medium. As an approach to a clarification of the role of laccases during the attack on lignin by the fungus, the enzyme has been characterized further. The levels of this phenol oxidase increase 2-fold in the presence of p-anisidine and are severely affected when addition of ...

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Manganese-Dependent Cleavage of Nonphenolic Lignin Structures by Ceriporiopsis subvermispora in the Absence of Lignin Peroxidase.

Many ligninolytic fungi appear to lack lignin peroxidase (LiP), the enzyme generally thought to cleave the major, recalcitrant, nonphenolic structures in lignin. At least one such fungus, Ceriporiopsis subvermispora, is nevertheless able to degrade these nonphenolic structures. Experiments showed that wood block cultures and defined liquid medium cultures of C. subvermispora rapidly depolymeriz...

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Modeling Based Structural Insights into Biodegradation of the Herbicide Diuron by Laccase-1 from Ceriporiopsis subvermispora

The herbicide diuron (3-(3,4-dichlorophenyl)-1,1-dimethylurea) is used in many agricultural crops and non-crop areas worldwide, leading to the pollution of the aquatic environment by soil leaching. White rot fungi and its lignin modifying enzymes, peroxidases and laccases, are responsible for its degradation. Therefore, it is of interest to explore the potential use of Ceriporiopsis subvermispo...

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Heterologous expression of laccase cDNA from Ceriporiopsis subvermispora yields copper-activated apoprotein and complex isoform patterns.

Analysis of genomic clones encoding a putative laccase in homokaryon strains of Ceriporiopsis subvermispora led to the identification of an allelic variant of the previously described lcs-1 gene. A cDNA clone corresponding to this gene was expressed in Aspergillus nidulans and in Aspergillus niger. Enzyme assays and Western blots showed that both hosts secreted active laccase. Relative to the i...

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ژورنال

عنوان ژورنال: Applied and Environmental Microbiology

سال: 1995

ISSN: 0099-2240,1098-5336

DOI: 10.1128/aem.61.3.872-876.1995